title: Backbone NMR assignments of a topologically knotted protein in urea-denatured state.
abstract: YbeA is a 3-methylpseudoridine methyltransferase from Escherichia coli that forms a stable homodimer in solution. It is one of the deeply trefoil 31 knotted proteins, of which the knot encompasses the C-terminal helix that threads through a long loop. Recent studies on the knotted protein folding pathways using YbeA have suggested that the protein knot remains present under chemically denaturing conditions. Here, we report (1)H, (13)C and (15)N chemical shift assignments for urea-denatured YbeA, which will serve as the basis for further structural characterisations using solution state NMR spectroscopy with paramagnetic spin labeled and partial alignment media.
authors.affiliation: Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.
authors.forename: Shu-Ju Micky
authors.initials: SJ
authors.lastname: Hsieh
authors.forename: Anna L
authors.initials: AL
authors.lastname: Mallam
authors.forename: Sophie E
authors.initials: SE
authors.lastname: Jackson
authors.forename: Shang-Te Danny
authors.initials: ST
authors.lastname: Hsu
mesh_terms: D004926:Escherichia coli / Q000201:enzymology; D029968:Escherichia coli Proteins / Q000737:chemistry*; D008780:Methyltransferases / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011489:Protein Denaturation / Q000187:drug effects*; D014508:Urea / Q000494:pharmacology*
chemical_list: D029968:Escherichia coli Proteins; D014508:Urea; D008780:Methyltransferases; C532170:RlmH protein, E coli